The role of the phosphorylation of various proteins associated with the protein synthesizing complex in translational control is currently being examined. Initiation factors and elongation factors phosphorylated in intact reticulocytes will be identified by two-dimensional polyacrylamide gel electrophoresis. The protein kinase and phosphoprotein phosphatase activities modifying these factors will be identified and purified. The aim of this study is a functional analysis of the phosphorylated components and an examination of the effects of these modifications on protein synthesis. This will be accomplished by analyzing the phosphorylated and dephosphorylated factors in conjunction with phosphorylated and dephosphorylated ribosomes in the various partial reactions of protein synthesis. In addition, the pattern of proteins phosphorylated in whole cells and in cell lysates will be examined under a variety of conditions which stimulate and inhibit protein synthesis. Some of the metabolic effectors to be studied include cyclic AMP, cyclic GMP, hemin, sodium fluoride, polyamines, and double stranded RNA.